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1URI

AZURIN MUTANT WITH MET 121 REPLACED BY GLN

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0009055molecular_functionelectron transfer activity
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0005507molecular_functioncopper ion binding
B0009055molecular_functionelectron transfer activity
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU A 200
ChainResidue
AGLY45
AHIS46
ACYS112
AHIS117
AGLN121

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 393
ChainResidue
AHOH238
AALA75
AGLY76
AHIS83
AHOH220

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU B 201
ChainResidue
BGLY45
BHIS46
BCYS112
BHIS117
BGLN121

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 394
ChainResidue
BVAL73
BLYS74
BALA75
BGLY76
BHIS83
BHOH248
BHOH258

Functional Information from PROSITE/UniProt
site_idPS00196
Number of Residues17
DetailsCOPPER_BLUE Type-1 copper (blue) proteins signature. GeaYaYFCsfPgHwam.Q
ChainResidueDetails
AGLY105-GLN121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues256
DetailsDomain: {"description":"Plastocyanin-like"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"3210236","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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